Ceramide very long chain fatty acid hydroxylase SCS7 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

Q03529 (SCS7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 120. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ceramide very long chain fatty acid hydroxylase SCS7
Short name=Ceramide VLCFA hydroxylase SCS7
EC=1.-.-.-

Alternative name(s):
Suppressor of calcium sensitivity 7

Gene names

Name:	SCS7
Synonyms:	FAH1
Ordered Locus Names:	YMR272C
ORF Names:	YM8156.14C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	384 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Ceramide hydroxylase involved in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids. Hydroxylates the very long chain fatty acid of ceramides at C2 and C3. Ref.4 Ref.5 Ref.6 Ref.7 Ref.11 Ref.12
Cofactor	Iron By similarity.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.8.
Domain	The histidine box domains may contain the active site and/or be involved in metal ion binding.
Miscellaneous	Present with 3290 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the sterol desaturase family. SCS7 subfamily. Contains 1 cytochrome b5 heme-binding domain.

Ontologies

Keywords
Biological process	Electron transport Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW fatty acid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW inositolphosphoceramide metabolic process Inferred from mutant phenotype Ref.11 Ref.4 Ref.5 Ref.6. Source: SGD
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.8. Source: SGD endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD
Molecular_function	fatty acid alpha-hydroxylase activity Inferred from mutant phenotype Ref.4 Ref.6. Source: SGD heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 384

384

Ceramide very long chain fatty acid hydroxylase SCS7

PRO_0000185407

Regions

Topological domain

1 – 196

196

Cytoplasmic Potential

Transmembrane

197 – 217

Helical; Potential

Topological domain

218 – 222

Lumenal Potential

Transmembrane

223 – 243

Helical; Potential

Topological domain

244 – 297

Cytoplasmic Potential

Transmembrane

298 – 318

Helical; Potential

Topological domain

319 – 352

Lumenal Potential

Transmembrane

353 – 373

Helical; Potential

Topological domain

374 – 384

Cytoplasmic Potential

Domain

9 – 90

Cytochrome b5 heme-binding

Sites

Metal binding

Iron (heme axial ligand) By similarity

Metal binding

Iron (heme axial ligand) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q03529 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: DF4BA5F2E0EA2218
Show »

FASTA

384

44,881

        10         20         30         40         50         60 
MSTNTSKTLE LFSKKTVQEH NTANDCWVTY QNRKIYDVTR FLSEHPGGDE SILDYAGKDI 

        70         80         90        100        110        120 
TEIMKDSDVH EHSDSAYEIL EDEYLIGYLA TDEEAARLLT NKNHKVEVQL SADGTEFDST 

       130        140        150        160        170        180 
TFVKELPAEE KLSIATDYSN DYKKHKFLDL NRPLLMQILR SDFKKDFYVD QIHRPRHYGK 

       190        200        210        220        230        240 
GSAPLFGNFL EPLTKTAWWV VPVAWLPVVV YHMGVALKNM NQLFACFLFC VGVFVWTLIE 

       250        260        270        280        290        300 
YGLHRFLFHF DDWLPESNIA FATHFLLHGC HHYLPMDKYR LVMPPTLFVI LCAPFYKLVF 

       310        320        330        340        350        360 
ALLPLYWAYA GFAGGLFGYV CYDECHFFLH HSKLPPFMRK LKKYHLEHHY KNYQLGFGVT 

       370        380 
SWFWDEVFGT YLGPDAPLSK MKYE

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"Fah1p, a Saccharomyces cerevisiae cytochrome b5 fusion protein, and its Arabidopsis thaliana homolog that lacks the cytochrome b5 domain both function in the alpha-hydroxylation of sphingolipid-associated very long chain fatty acids." Mitchell A.G., Martin C.E. J. Biol. Chem. 272:28281-28288(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[5]	"Hydroxylation of Saccharomyces cerevisiae ceramides requires Sur2p and Scs7p." Haak D., Gable K., Beeler T., Dunn T. J. Biol. Chem. 272:29704-29710(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Synthesis of monohydroxylated inositolphosphorylceramide (IPC-C) in Saccharomyces cerevisiae requires Scs7p, a protein with both a cytochrome b5-like domain and a hydroxylase/desaturase domain." Dunn T.M., Haak D., Monaghan E., Beeler T.J. Yeast 14:311-321(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Sterol-dependent regulation of sphingolipid metabolism in Saccharomyces cerevisiae." Swain E., Baudry K., Stukey J., McDonough V., Germann M., Nickels J.T. Jr. J. Biol. Chem. 277:26177-26184(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]	"A global topology map of the Saccharomyces cerevisiae membrane proteome." Kim H., Melen K., Oesterberg M., von Heijne G. Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract] Cited for: TOPOLOGY [LARGE SCALE ANALYSIS]. Strain: ATCC 208353 / W303-1A.
[11]	"Mass spectrometry-based profiling of phospholipids and sphingolipids in extracts from Saccharomyces cerevisiae." Guan X.L., Wenk M.R. Yeast 23:465-477(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Incorporation of ceramides into Saccharomyces cerevisiae glycosylphosphatidylinositol-anchored proteins can be monitored in vitro." Bosson R., Guillas I., Vionnet C., Roubaty C., Conzelmann A. Eukaryot. Cell 8:306-314(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z49260 Genomic DNA. Translation: CAA89255.1. AY693150 Genomic DNA. Translation: AAT93169.1. BK006946 Genomic DNA. Translation: DAA10172.1.
PIR	S54484.
RefSeq	NP_013999.1. NM_001182779.1.
3D structure databases
ProteinModelPortal	Q03529.
SMR	Q03529. Positions 13-85.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q03529. 34 interactions.
MINT	MINT-4498866.
STRING	4932.YMR272C.
Proteomic databases
PaxDb	Q03529.
PeptideAtlas	Q03529.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR272C; YMR272C; YMR272C.
GeneID	855315.
KEGG	sce:YMR272C.
Organism-specific databases
CYGD	YMR272c.
SGD	S000004885. SCS7.
Phylogenomic databases
eggNOG	COG3000.
GeneTree	ENSGT00390000002142.
HOGENOM	HOG000023981.
OMA	SEYWHWI.
OrthoDB	EOG49S9FT.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13537.
Gene expression databases
Genevestigator	Q03529.
GermOnline	YMR272C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.10.120.10. 1 hit.
InterPro	IPR001199. Cyt_B5-like_heme/steroid-bd. IPR018506. Cyt_B5_heme-BS. IPR006694. Fatty_acid_hydroxylase. IPR014430. Ino-phos-ceramide-B_Hydrxlase. [Graphical view]
Pfam	PF00173. Cyt-b5. 1 hit. PF04116. FA_hydroxylase. 1 hit. [Graphical view]
PIRSF	PIRSF005149. IPC-B_HD. 1 hit.
PRINTS	PR00363. CYTOCHROMEB5.
SUPFAM	SSF55856. Cyt_B5. 1 hit.
PROSITE	PS00191. CYTOCHROME_B5_1. 1 hit. PS50255. CYTOCHROME_B5_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	979008.

Entry information

Entry name

SCS7_YEAST

Accession

Primary (citable) accession number: Q03529
Secondary accession number(s): D6W098

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 120 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents